ID   DNAK_AKKM8              Reviewed;         642 AA.
AC   B2UKV6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Amuc_1406;
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC   107961 / Muc;
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; CP001071; ACD05229.1; -; Genomic_DNA.
DR   RefSeq; WP_012420444.1; NC_010655.1.
DR   AlphaFoldDB; B2UKV6; -.
DR   SMR; B2UKV6; -.
DR   STRING; 349741.Amuc_1406; -.
DR   PRIDE; B2UKV6; -.
DR   EnsemblBacteria; ACD05229; ACD05229; Amuc_1406.
DR   GeneID; 60880883; -.
DR   KEGG; amu:Amuc_1406; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OMA; KRQGVVN; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; AMUC349741:G1GBX-1497-MON; -.
DR   Proteomes; UP000001031; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119660"
FT   REGION          600..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   642 AA;  68854 MW;  6E08D2CDE67B95EA CRC64;
     MAKILGIDLG TTNSCMAVME GGQGTVLENS EGARTTPSIV AFTKSGERLV GQAAKRQAVT
     NPKNTVFSSK RLIGRKYSEL TEEDKKVPYE IVEAPNGDAY IRVDVGGEKK TFSPQEIASM
     VLAKLKADAE SKLGETITEA VITVPAYFND AQRNATKAAG EIAGLKVRRI INEPTAAALA
     YGLDKKSNEN IAVYDLGGGT FDISVLEIGD GVFEVKASDG DTHLGGDDWD NAIINWIIGE
     FKKDSGMDLS NQPDAIQRIK EEAEKAKIAL SSTQSYDISL PFITADASGP KHIQLTLSRP
     KLEQLTEDLL DRTRKPVLDC IAASGLKTGD IDELVLVGGM TRMPAVQEMA HTLAGKEPHK
     GVNPDEVVAL GAAIQGGVLQ GDVNDVLLLD VTPLTLSIET MGGIATPMIE RNTTIPVRKS
     QVFSTAADNQ PAVDIRICQG ERKMFEDNKL LGNFKLDGIS PAPRGVPQIE VTFDIDANGI
     LHVSAKDKGT GKEQKISIQG SSGLSKDEIE RAKRDAEAHA EEDKKRAEEI DTINQADSLC
     FSVERQLKDM GDKLPADLKR EIEDKVTRLK EAVSKKDVTA IKAGKEDLES RLEALYKAAE
     AAQQSAGAAG PMPGAPAEEE PSDGPRKAKG RVVDAEIVDD DK